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Protein

ATP-dependent RNA helicase ded1

Gene

ded1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

ATP-binding RNA helicase involved in translation initiation. Remodels RNA in response to ADP and ATP concentrations by facilitating disruption, but also formation of RNA duplexes (By similarity). Inactivation of ded1 blocks mitotic cell cycle progression at G1 and G2/M. Induces sexual development and ascus formation.By similarity3 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi213 – 220ATPPROSITE-ProRule annotation8

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ATP-dependent RNA helicase activity Source: PomBase
  • translation initiation factor activity Source: PomBase

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • chromosome segregation Source: GO_Central
  • cytoplasmic translational initiation Source: PomBase
  • gene silencing by RNA Source: UniProtKB
  • mitotic nuclear division Source: UniProtKB-KW
  • regulation of gene expression Source: GO_Central
  • RNA secondary structure unwinding Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase, Initiation factor

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Enzyme and pathway databases

ReactomeiR-SPO-6798695. Neutrophil degranulation.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent RNA helicase ded1 (EC:3.6.4.13)
Alternative name(s):
Multicopy suppressor of overexpressed cyr1 protein 2
Gene namesi
Name:ded1
Synonyms:dep1, moc2, sum3
ORF Names:SPCC1795.11
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:SPCC1795.11.
PomBaseiSPCC1795.11.

Subcellular locationi

GO - Cellular componenti

  • cytoplasmic ribonucleoprotein granule Source: GO_Central
  • cytosol Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000550421 – 636ATP-dependent RNA helicase ded1Add BLAST636

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei52Phosphoserine1 Publication1
Modified residuei54Phosphoserine1 Publication1
Modified residuei55Phosphoserine1 Publication1
Modified residuei58Phosphoserine1 Publication1
Modified residuei59Phosphoserine1 Publication1
Modified residuei63Phosphothreonine1 Publication1
Modified residuei128Phosphothreonine1 Publication1
Modified residuei312Phosphothreonine1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO13370.
PRIDEiO13370.

PTM databases

iPTMnetiO13370.

Interactioni

Subunit structurei

Interacts with chk1, which is required for cell cycle arrest following DNA damage.

Binary interactionsi

WithEntry#Exp.IntActNotes
rkp1Q102813EBI-2478405,EBI-696304
rpl3202P790153EBI-2478405,EBI-7169357

Protein-protein interaction databases

BioGridi275274. 36 interactors.
IntActiO13370. 11 interactors.
MINTiMINT-4666622.

Structurei

3D structure databases

ProteinModelPortaliO13370.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini200 – 392Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST193
Domaini403 – 564Helicase C-terminalPROSITE-ProRule annotationAdd BLAST162

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi169 – 197Q motifAdd BLAST29
Motifi336 – 339DEAD box4

Domaini

The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.

Sequence similaritiesi

Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000268804.
InParanoidiO13370.
KOiK11594.
OMAiFFNSENS.
OrthoDBiEOG092C1B4A.
PhylomeDBiO13370.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O13370-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDNVQQQVD SVGSVTEKLQ KTNISRPRKY IPPFARDKPS AGAAPAVGDD
60 70 80 90 100
ESVSSRGSSR SQTPSEFSSN YGGRREYNRG GHYGGGEGRQ NNYRGGREGG
110 120 130 140 150
YSNGGGYRNN RGFGQWRDGQ HVIGARNTLL ERQLFGAVAD GTKVSTGINF
160 170 180 190 200
EKYDDIPVEV SGGDIEPVNE FTSPPLNSHL LQNIKLSGYT QPTPVQKNSI
210 220 230 240 250
PIVTSGRDLM ACAQTGSGKT AGFLFPILSL AFDKGPAAVP VDQDAGMGYR
260 270 280 290 300
PRKAYPTTLI LAPTRELVCQ IHEESRKFCY RSWVRPCAVY GGADIRAQIR
310 320 330 340 350
QIDQGCDLLS ATPGRLVDLI DRGRISLANI KFLVLDEADR MLDMGFEPQI
360 370 380 390 400
RHIVEGADMT SVEERQTLMF SATFPRDIQL LARDFLKDYV FLSVGRVGST
410 420 430 440 450
SENITQKVVH VEDSEKRSYL LDILHTLPPE GLTLIFVETK RMADTLTDYL
460 470 480 490 500
LNSNFPATSI HGDRTQRERE RALELFRSGR TSIMVATAVA SRGLDIPNVT
510 520 530 540 550
HVINYDLPTD IDDYVHRIGR TGRAGNTGQA VAFFNRNNKG IAKELIELLQ
560 570 580 590 600
EANQECPSFL IAMARESSFG GNGRGGRYSG RGGRGGNAYG ARDFRRPTNS
610 620 630
SSGYSSGPSY SGYGGFESRT PHHGNTYNSG SAQSWW
Length:636
Mass (Da):69,759
Last modified:January 1, 1998 - v1
Checksum:i094630A41A3C26F1
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti41A → R in BAA25324 (PubMed:10395922).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF025536 mRNA. Translation: AAC04893.1.
AF084222 Genomic DNA. Translation: AAC34121.1.
AB012389 mRNA. Translation: BAA25324.1.
AJ237697 mRNA. Translation: CAB40192.1.
CU329672 Genomic DNA. Translation: CAA18646.1.
AB027871 Genomic DNA. Translation: BAA87175.1.
PIRiT43543.
RefSeqiNP_588033.1. NM_001023025.2.

Genome annotation databases

EnsemblFungiiSPCC1795.11.1; SPCC1795.11.1:pep; SPCC1795.11.
GeneIDi2538689.
KEGGispo:SPCC1795.11.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF025536 mRNA. Translation: AAC04893.1.
AF084222 Genomic DNA. Translation: AAC34121.1.
AB012389 mRNA. Translation: BAA25324.1.
AJ237697 mRNA. Translation: CAB40192.1.
CU329672 Genomic DNA. Translation: CAA18646.1.
AB027871 Genomic DNA. Translation: BAA87175.1.
PIRiT43543.
RefSeqiNP_588033.1. NM_001023025.2.

3D structure databases

ProteinModelPortaliO13370.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi275274. 36 interactors.
IntActiO13370. 11 interactors.
MINTiMINT-4666622.

PTM databases

iPTMnetiO13370.

Proteomic databases

MaxQBiO13370.
PRIDEiO13370.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPCC1795.11.1; SPCC1795.11.1:pep; SPCC1795.11.
GeneIDi2538689.
KEGGispo:SPCC1795.11.

Organism-specific databases

EuPathDBiFungiDB:SPCC1795.11.
PomBaseiSPCC1795.11.

Phylogenomic databases

HOGENOMiHOG000268804.
InParanoidiO13370.
KOiK11594.
OMAiFFNSENS.
OrthoDBiEOG092C1B4A.
PhylomeDBiO13370.

Enzyme and pathway databases

ReactomeiR-SPO-6798695. Neutrophil degranulation.

Miscellaneous databases

PROiO13370.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDED1_SCHPO
AccessioniPrimary (citable) accession number: O13370
Secondary accession number(s): O59857, Q9UU14
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: January 1, 1998
Last modified: November 30, 2016
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

A different form of ded1 has been identified via SDS-PAGE studies. It is uncertain how this form arises in vivo.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.